Encapsulating Subsite analogues of the [FeFe]-hydrogenases in micelles enables direct water interactions
| Autor: | Joseph A. Wright, Robby Fritzsch, Owen Brady, Christopher J. Pickett, Elaine Adair, Neil T. Hunt |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
Heptane
Aqueous solution Inorganic chemistry Supramolecular chemistry Infrared spectroscopy 02 engineering and technology 010402 general chemistry 021001 nanoscience & nanotechnology Photochemistry 01 natural sciences Micelle 0104 chemical sciences QD450 chemistry.chemical_compound chemistry Molecule General Materials Science Microemulsion Physical and Theoretical Chemistry 0210 nano-technology Spectroscopy |
| ISSN: | 1948-7185 |
| Popis: | Encapsulation of subsite analogues of the [FeFe]-hydrogenase enzymes in supramolecular structures has been shown to dramatically increase their catalytic ability, but the molecular basis for this enhancement remains unclear. We report the results of experiments employing infrared absorption, ultrafast infrared pump-probe, and 2D-IR spectroscopy to investigate the molecular environment of Fe2(pdt)(CO)6 (pdt: propanedithiolate) [1] encapsulated in the dispersed alkane phase of a heptane-dodecyltrimethylammonium bromide-water microemulsion. It is demonstrated that 1 is partitioned between two molecular environments, one that closely resembles bulk heptane solution and a second that features direct hydrogen-bonding interactions with water molecules that penetrate the surfactant shell. Our results demonstrate that the extent of water access to the normally water-insoluble subsite analogue 1 can be tuned with micelle size, while IR spectroscopy provides a straightforward tool that can be used to measure and fine-tune the chemical environment of catalyst species in self-assembled structures. |
| Databáze: | OpenAIRE |
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